Mitochondrial protein p32 can accumulate in the nucleus

K A Brokstad, K H Kalland, W C Russell, D A Matthews

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)

Abstract

Human p32 was first isolated associated with the splicing factor ASF/SF-2, The p32 protein is translated as pre-protein from which a mitochondrial import signal is cleaved off to create the mature p32. The majority of p32 is consequently found in the mitochondria. In this study we investigated extramitochondrial p32. An increased nuclear localisation of endogenous p32 was demonstrated as a response to leptomycin B or actinomycin D treatment of cells. Mature p32 gene and deletion mutants were cloned into enhanced green fluorescence protein reporter plasmids. On transfection, EGFP-p32 protein was mainly localised to the cytoplasm and to a lesser extent to the nucleus of transfected COS cells. Upon treatment with actinomycin D or leptomycin B, the EGFP-p32 protein accumulated in the nucleus. Deletion analysis indicated which regions of EGFP-p32 are involved in nuclear export and nuclear import. (C) 2001 Academic Press.

Original languageEnglish
Pages (from-to)1161-1169
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume281
Publication statusPublished - 16 Mar 2001

Keywords

  • p32
  • splicing associated protein
  • mitochondrial protein
  • actinomycin D (act. D)
  • leptomycin B (LMB)
  • IMMUNODEFICIENCY-VIRUS TYPE-1
  • RNA-BINDING-PROTEINS
  • IN-VITRO INTERACTION
  • SPLICING FACTOR
  • ACTIVATION DOMAIN
  • CELLULAR PROTEIN
  • REV PROTEIN
  • TAT TRANSACTIVATOR
  • MESSENGER-RNA
  • P-32 PROTEIN

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